2vla



CRYSTAL STRUCTURE OF RESTRICTION ENDONUCLEASE BPUJI RECOGNITION DOMAIN IN COMPLEX WITH COGNATE DNA

Overview
Type IIS restriction endonucleases recognize asymmetric DNA sequences and cleave both DNA strands at fixed positions downstream of the recognition site. The restriction endonuclease BpuJI recognizes the asymmetric sequence 5'-CCCGT; however, it cuts at multiple sites in the vicinity of the target sequence. BpuJI consists of two physically separate domains, with catalytic and dimerization functions in the C-terminal domain and DNA recognition functions in the N-terminal domain. This is the crystal structure of the BpuJI recognition domain bound to cognate DNA at 1.3-A resolution. This region folds into two winged-helix subdomains, D1 (red) and D2 (blue), interspaced by the DL subdomain (green)TextToBeDisplayed. The D1 and D2 subdomains of BpuJI share structural similarity with the similar subdomains of the FokI DNA-binding domain; however, their orientations in protein-DNA complexes are different. Recognition of the 5'-CCCGT target sequence is achieved by BpuJI through the major groove contacts of amino acid residues located on both the helix-turn-helix motifs and the N-terminal arm (magenta).

About this Structure
2VLA is a Protein complex structure of sequences from Bacillus pumilus. Full crystallographic information is available from OCA.

Reference
The recognition domain of the BpuJI restriction endonuclease in complex with cognate DNA at 1.3-A resolution., Sukackaite R, Grazulis S, Bochtler M, Siksnys V, J Mol Biol. 2008 May 16;378(5):1084-93. Epub 2008 Mar 28. PMID:18433771

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